Pathways & interactions
Glutamine synthetase/guanido kinase, catalytic domain (IPR014746)
Short name: Gln_synth/guanido_kin_cat_dom
- ATP:guanido phosphotransferase (IPR000749)
- Glutamine synthetase class-I, adenylation site (IPR001637)
- Glutamate-cysteine ligase catalytic subunit (IPR004308)
- Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit (IPR004413)
- Glutamyl-tRNA(Gln) amidotransferase subunit E (IPR004414)
- Glutamine synthetase type I (IPR004809)
- Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic (IPR006075)
- Glutamate--cysteine ligase, monofunctional (IPR006334)
- Glutathione biosynthesis bifunctional protein GshAB (IPR006335)
- Glutamate--cysteine ligase, GCS2 (IPR006336)
- Glutamate--cysteine ligase (IPR007370)
- Glutamine synthetase, catalytic domain (IPR008146)
- Glutamate--cysteine ligase, plant-type (IPR011556)
- Glutamate--cysteine ligase, putative (IPR011792)
- Putative glutamate--cysteine ligase YbdK (IPR011793)
- Uncharacterised conserved protein UCP012666 (IPR016602)
- Glutamine synthetase, type III (IPR017536)
- Glutamate--cysteine ligase EgtA, Actinobacteria (IPR017809)
- Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site (IPR017958)
- Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E (IPR017959)
- ATP:guanido phosphotransferase, catalytic domain (IPR022414)
- ATP:guanido phosphotransferase active site (IPR022415)
- Protein arginine kinase (IPR023660)
- Glutamine synthetase, glycine-rich site (IPR027303)
- Glutamate--cysteine ligase, bacteria and plant (IPR035434)
- Glutamine synthetase, C-terminal (IPR040577)
The C-terminal catalytic domains of glutamine synthetase and the guanido kinase family (which includes creatine kinase and arginine kinase) share a common structural fold, namely a common core consisting of two beta-alpha-beta2-alpha repeats [PMID: 9434900].
Glutamine synthetase (EC:220.127.116.11) (GS) [PMID: 9559050] plays an essential role in the metabolism of nitrogen by catalysing the condensation of glutamate and ammonia to form glutamine. There seem to be three different classes of GS [PMID: 8096645, PMID: 2575672, PMID: 7916055]. Class I enzymes (GSI) are specific to prokaryotes, and are oligomers of 12 identical subunits; the activity of GSI-type enzyme is controlled by the adenylation of a tyrosine residue. Class II enzymes (GSII) are found in eukaryotes and in bacteria, and are oligomers of 8 identical subunits. Class III enzymes (GSIII) have been found in Bacteroides fragilis in Butyrivibrio fibrisolvens, and are oligomers of six identical subunits. While the three classes of GS's are clearly structurally related, the sequence similarities are not so extensive.
ATP:guanido phosphotransferases are a family of structurally and functionally related enzymes [PMID: 2324092, PMID: 7819288] that reversibly catalyse the transfer of phosphate between ATP and various phosphogens. The enzymes belonging to this family include:
- Glycocyamine kinase (EC:18.104.22.168), which catalyses the transfer of phosphate from ATP to guanidoacetate.
- Arginine kinase (EC:22.214.171.124), which catalyses the transfer of phosphate from ATP to arginine.
- Taurocyamine kinase (EC:126.96.36.199), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to taurocyamine.
- Lombricine kinase (EC:188.8.131.52), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to lombricine.
- Smc74, a cercaria-specific enzyme from Schistosoma mansoni [PMID: 2324092].
- Creatine kinase (EC:184.108.40.206) (CK) [PMID: 3896131, PMID: 2324105], which plays an important role in energy metabolism of vertebrates.
No terms assigned in this category.
GO:0003824 catalytic activity
No terms assigned in this category.
- SSF55931 (SSF55931)